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Conserved domains on  [gi|1064290784|gb|AOP03673|]
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Choline kinase [Streptococcus suis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LicC super family cl44122
CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid ...
 4-209 5.21e-55

CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


The actual alignment was detected with superfamily member COG4750:

Pssm-ID: 443784 [Multi-domain]  Cd Length: 228  Bit Score: 184.26  E-value: 5.21e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784   4 KNAIILAAGLGRRTIPLNFETHKAFLEVNGEILIERLIVQLKEAGVSEIIIVIGYKKEQFRYLIDKYEVELIENDDFANS 83
Cdd:COG4750     1 MNAIILAAGLGSRFAPITYETPKGLLKVNGEPLIERQIRQLHEAGITDITVVVGYLKEQFEYLEDKYGVKLIYNPDYAEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784  84 NTLYSLSLAESYLSNSYIIPCDIWCATNPFtSKKDDSSWYMI-----------------GDISKSVTKLDNLSERLAVAF 146
Cdd:COG4750    81 NNISSLYLVRDKLGNTYICSSDNYLTENPF-EKYEYKSYYSAvykegetdewcvktnrdGRITKIEIGGKDGWIMLGHSY 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1064290784 147 IEQSDSIWIKQRLRELANNPSQQMLAWEELLVTD-GELAIPTFKNCEHFIQDINTFEDLIYLDD 209
Cdd:COG4750   160 WDKEDSKKFKEILEEEYEDPETRDLYWEDIYMDHiDELDMYARKYPAGDIYEFDSLDELREFDP 223
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
 234-434 2.01e-50

Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic choline kinases, as well as eukaryotic ethanolamine kinase. ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC), and sphingomyelin (SM). Although choline is the preferred substrate, ChoK also shows substantial activity towards ethanolamine and its N-methylated derivatives. Bacterial ChoK is also referred to as licA protein. ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate and displays negligible activity towards N-methylated derivatives of Etn. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. The ChoK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


:

Pssm-ID: 270700 [Multi-domain]  Cd Length: 152  Bit Score: 169.27  E-value: 2.01e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784 234 KNVFALKKGMTNRSFMFECKDKSYIMRIPGEGTDKLINREQEAEVYRVIAGESISDELIYISPEKGYKITSFIDGARNCD 313
Cdd:cd05151     1 ITIEPLKGGLTNKNYLVEVAGKKYVLRIPGAGTELLIDRENEKANSKAAAELGIAPEVIYFDPETGVKITEFIEGATLLT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784 314 SN--NKSDVSLCMKKLRSFHerglttshefdlfgeiefyeslrgnresiyedyqsvknrvltlksyiQLNIEKKVLCHID 391
Cdd:cd05151    81 NDfsDPENLERIAALLRKLH-----------------------------------------------SSPLEDLVLCHND 113

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1064290784 392 ANPDNFLIfeknNQTEVRLIDWEYAGMQDPDLDIAMFAIYSQY 434
Cdd:cd05151   114 LVPGNFLL----DDDRLYLIDWEYAGMNDPLFDLAALFSENNL 152
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
340-492 3.91e-33

Thiamine kinase or a related kinase [Coenzyme transport and metabolism];


:

Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 123.35  E-value: 3.91e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784 340 EFDLFGEIEFYESLRgnresiYEDYQSVKNRVLTLKSYIQLNIEKKVLCHIDANPDNFLIfekNNQTEVRLIDWEYAGMQ 419
Cdd:COG0510    10 RFDLFARLERYLALG------PRDLPELLRRLEELERALAARPLPLVLCHGDLHPGNFLV---TDDGRLYLIDWEYAGLG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1064290784 420 DPDLDIAMFAIYSQYNREQIDFLIGAYFEEGCEERIRMKIYAYVATAGLLWSNWCEYK--QQLGVEFGDYAQSQY 492
Cdd:COG0510    81 DPAFDLAALLVEYGLSPEQAEELLEAYGFGRPTEELLRRLRAYRALADLLWALWALVRaaQEANGDLLKYLLRRL 155
 
Name Accession Description Interval E-value
LicC COG4750
CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid ...
 4-209 5.21e-55

CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


Pssm-ID: 443784 [Multi-domain]  Cd Length: 228  Bit Score: 184.26  E-value: 5.21e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784   4 KNAIILAAGLGRRTIPLNFETHKAFLEVNGEILIERLIVQLKEAGVSEIIIVIGYKKEQFRYLIDKYEVELIENDDFANS 83
Cdd:COG4750     1 MNAIILAAGLGSRFAPITYETPKGLLKVNGEPLIERQIRQLHEAGITDITVVVGYLKEQFEYLEDKYGVKLIYNPDYAEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784  84 NTLYSLSLAESYLSNSYIIPCDIWCATNPFtSKKDDSSWYMI-----------------GDISKSVTKLDNLSERLAVAF 146
Cdd:COG4750    81 NNISSLYLVRDKLGNTYICSSDNYLTENPF-EKYEYKSYYSAvykegetdewcvktnrdGRITKIEIGGKDGWIMLGHSY 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1064290784 147 IEQSDSIWIKQRLRELANNPSQQMLAWEELLVTD-GELAIPTFKNCEHFIQDINTFEDLIYLDD 209
Cdd:COG4750   160 WDKEDSKKFKEILEEEYEDPETRDLYWEDIYMDHiDELDMYARKYPAGDIYEFDSLDELREFDP 223
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
 234-434 2.01e-50

Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic choline kinases, as well as eukaryotic ethanolamine kinase. ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC), and sphingomyelin (SM). Although choline is the preferred substrate, ChoK also shows substantial activity towards ethanolamine and its N-methylated derivatives. Bacterial ChoK is also referred to as licA protein. ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate and displays negligible activity towards N-methylated derivatives of Etn. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. The ChoK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270700 [Multi-domain]  Cd Length: 152  Bit Score: 169.27  E-value: 2.01e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784 234 KNVFALKKGMTNRSFMFECKDKSYIMRIPGEGTDKLINREQEAEVYRVIAGESISDELIYISPEKGYKITSFIDGARNCD 313
Cdd:cd05151     1 ITIEPLKGGLTNKNYLVEVAGKKYVLRIPGAGTELLIDRENEKANSKAAAELGIAPEVIYFDPETGVKITEFIEGATLLT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784 314 SN--NKSDVSLCMKKLRSFHerglttshefdlfgeiefyeslrgnresiyedyqsvknrvltlksyiQLNIEKKVLCHID 391
Cdd:cd05151    81 NDfsDPENLERIAALLRKLH-----------------------------------------------SSPLEDLVLCHND 113

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1064290784 392 ANPDNFLIfeknNQTEVRLIDWEYAGMQDPDLDIAMFAIYSQY 434
Cdd:cd05151   114 LVPGNFLL----DDDRLYLIDWEYAGMNDPLFDLAALFSENNL 152
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 6-204 7.26e-35

Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.


Pssm-ID: 133014 [Multi-domain]  Cd Length: 229  Bit Score: 130.43  E-value: 7.26e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784   6 AIILAAGLGRRTIPLNFETHKAFLEVNGEILIERLIVQLKEAGVSEIIIVIGYKKEQFRYLIDKY-EVELIENDDFANSN 84
Cdd:cd02523     1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYpNIKFVYNPDYAETN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784  85 TLYSLSLAESYLS-NSYIIPCDIWCATNPF------------------------TSKKDDSSWYMIGDISKSVTKLDNLS 139
Cdd:cd02523    81 NIYSLYLARDFLDeDFLLLEGDVVFDPSILerllsspadnailvdkktkewedeYVKDLDDAGVLLGIISKAKNLEEIQG 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1064290784 140 ERLAVAFIEQSDSIWIKQRLRELANNPSQQMLaWEEL---LVTDGELAIptfKNCE-HFIQDINTFEDL 204
Cdd:cd02523   161 EYVGISKFSPEDADRLAEALEELIEAGRVNLY-YEDAlqrLISEEGVKV---KDISdGFWYEIDDLEDL 225
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
340-492 3.91e-33

Thiamine kinase or a related kinase [Coenzyme transport and metabolism];


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 123.35  E-value: 3.91e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784 340 EFDLFGEIEFYESLRgnresiYEDYQSVKNRVLTLKSYIQLNIEKKVLCHIDANPDNFLIfekNNQTEVRLIDWEYAGMQ 419
Cdd:COG0510    10 RFDLFARLERYLALG------PRDLPELLRRLEELERALAARPLPLVLCHGDLHPGNFLV---TDDGRLYLIDWEYAGLG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1064290784 420 DPDLDIAMFAIYSQYNREQIDFLIGAYFEEGCEERIRMKIYAYVATAGLLWSNWCEYK--QQLGVEFGDYAQSQY 492
Cdd:COG0510    81 DPAFDLAALLVEYGLSPEQAEELLEAYGFGRPTEELLRRLRAYRALADLLWALWALVRaaQEANGDLLKYLLRRL 155
Choline_kinase pfam01633
Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of ...
 253-428 9.45e-17

Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of phosphatidylcholine by the CDP-choline pathway. This alignment covers the protein kinase portion of the protein. The divergence of this family makes it very difficult to create a model that specifically predicts choline/ethanolamine kinases only. However if [add Pfam ID here for Choline_kinase_C] is also present then it is definitely a member of this family.


Pssm-ID: 396278 [Multi-domain]  Cd Length: 211  Bit Score: 78.85  E-value: 9.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784 253 KDKSYIMRIPGEGTDKLINREQEAEVYRVIAGESISDELIYISPEKGykITSFIDG-ARNCDSNNKSDVSLCM-KKLRSF 330
Cdd:pfam01633   1 SPRKVLLRIYGPGTELLINREDEIVNFALLSERGLGPKLYGFFPNGR--IEEFIPSrTLSTEDLRDPEISKLIaKRLAEL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784 331 HERGLTTSHEFDLFGEIEFYESL---RGNRESI-------YEDYQSVKNRVLTLKSYIQLNIEKKVLCHIDANPDNFLif 400
Cdd:pfam01633  79 HSLEMPGKKSPSLWKTMRKWLSLlknLGAPESVnkseqlkSINLEDLEKEINKLEKWLELLDSPIVFCHNDLQSGNIL-- 156

                         170       180
                  ....*....|....*....|....*...
gi 1064290784 401 EKNNQTEVRLIDWEYAGMQDPDLDIAMF 428
Cdd:pfam01633 157 LLNETKRLVLIDFEYASYNYRGFDIANH 184
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 6-106 1.17e-11

MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 62.98  E-value: 1.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784   6 AIILAAGLGRRtiplnFETHKAFLEVNGEILIERLIVQLKEAGvSEIIIVIGYkkEQFRYLIDKYEVELIENDDFAnSNT 85
Cdd:pfam12804   1 AVILAGGRSSR-----MGGDKALLPLGGKPLLERVLERLRPAG-DEVVVVAND--EEVLAALAGLGVPVVPDPDPG-QGP 71

                          90       100
                  ....*....|....*....|....
gi 1064290784  86 LYSLSLAESYLSNS---YIIPCDI 106
Cdd:pfam12804  72 LAGLLAALRAAPGAdavLVLACDM 95
ycfN_thiK TIGR02721
thiamine kinase; Members of this family are the ycfN gene product of Escherichia coli, now ...
 236-446 2.42e-10

thiamine kinase; Members of this family are the ycfN gene product of Escherichia coli, now identified as the salvage enzyme thiamine kinase (thiK), and additional proteobacterial homologs taken to be orthologs with equivalent function. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 274268 [Multi-domain]  Cd Length: 256  Bit Score: 60.88  E-value: 2.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784 236 VFALKKGMTNRSFMFECKDKSYIMRIPGEGTDKL-INREQEAEVYRVIAGESISDELIYISPekGYKITSFIDGARNCDS 314
Cdd:TIGR02721   1 VQTLSGGLTNRSWRIEHPGISFVWRPQSPVCKALgVDRQREYQILQALSALGLAPKPILVNE--HWLLVEWLEGEVITLD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784 315 NNKSDVSLC--MKKLRSFHERGLTtSHEFDLFGEIEFY-ESLRGNR-----ESIYEDYQSVKnrvltLKSYIQLniekkV 386
Cdd:TIGR02721  79 QFVALDLLLelAALLHQLHSQPRF-GYPLSLKARIAHYwLQIDPARrtpewLRLYKQFRSAP-----EPAPLPL-----A 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784 387 LCHIDANPDNFLIFEKNnqteVRLIDWEYAGMQDPDLDIAmfAIYSQYNREQIDFLIGAY 446
Cdd:TIGR02721 148 PLHMDVHAYNLVVTPQG----LKLIDWEYASDGDIALELA--AIIRANDEEQQQDFVQRY 201
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
 239-448 5.01e-06

Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction only];


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 48.19  E-value: 5.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784 239 LKKGMTNRSFMFECkDKSYIMRIPGEGTDKLINREQEAEVYRVIAGES----------ISDELIYISPekgYKITSFIDG 308
Cdd:COG3173    28 LSGGWSNLTYRLDT-GDRLVLRRPPRGLASAHDVRREARVLRALAPRLgvpvprplalGEDGEVIGAP---FYVMEWVEG 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784 309 ---ARNCDSNNKSDVSLCMKK----LRSFH-----ERGLTTSHEFDLFGEIEFYESLRGNRESIYEDYQSVKNRVLTlks 376
Cdd:COG3173   104 etlEDALPDLSPAERRALARAlgefLAALHavdpaAAGLADGRPEGLERQLARWRAQLRRALARTDDLPALRERLAA--- 180

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1064290784 377 YIQLNI---EKKVLCHIDANPDNfLIFEKNNQTEVRLIDWEYAGMQDPDLDIAMFAIYSQYN---REQIDFLIGAYFE 448
Cdd:COG3173   181 WLAANLpewGPPVLVHGDLRPGN-LLVDPDDGRLTAVIDWELATLGDPAADLAYLLLYWRLPddlLGPRAAFLAAYEE 257
thiK PRK10271
thiamine kinase; Provisional
 389-481 2.50e-05

thiamine kinase; Provisional


Pssm-ID: 182349  Cd Length: 188  Bit Score: 45.12  E-value: 2.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784 389 HIDANPDNFLIfeknNQTEVRLIDWEYAGMQDPDLDIAMFAIYSQYNREQidfLIGAYFEEG--CEERIRMKIYAYVATA 466
Cdd:PRK10271   81 HMDVHAGNLVH----SASGLRLIDWEYAGDGDIALELAAVWVENTEQHRQ---LVNDYATRAkiDAAQLWRQVRRWFPWV 153

                          90
                  ....*....|....*.
gi 1064290784 467 GLLWSNWCEYK-QQLG 481
Cdd:PRK10271  154 LMLKAGWFEYRwRQTG 169
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-62 4.46e-05

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 45.98  E-value: 4.46e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1064290784   4 KNAIILAAGLGRRtipLNFETHKAFLEVNGEILIERLIVQLKEAGVSEIIIVIGYKKEQ 62
Cdd:PRK14354    3 RYAIILAAGKGTR---MKSKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEE 58
PLN02421 PLN02421
phosphotransferase, alcohol group as acceptor/kinase
 242-426 5.16e-03

phosphotransferase, alcohol group as acceptor/kinase


Pssm-ID: 215231 [Multi-domain]  Cd Length: 330  Bit Score: 38.95  E-value: 5.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784 242 GMTNRSFMFECKDK-----SYIMRIPGEGTDKLINREQEAEVYRVIAGESISDELIYISpeKGYKITSFIDgARNCDSNN 316
Cdd:PLN02421   25 GITNLLLKVSVKEEngnevSVTVRLFGPNTDYVIDRERELQAIKYLSAAGFGAKLLGVF--GNGMIQSFIN-ARTLTPSD 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784 317 KSD---VSLCMKKLRSFHERGLTTSHEFDLFGEI-EFYESLRG------NRESIYED--YQSVKNRVLTLKSYIQLNIEK 384
Cdd:PLN02421  102 MRKpkvAAEIAKELRRLHQVEIPGSKEPQLWNDIfKFYEKASTvkfedpEKQKKYETisFEELRDEIVELKEITDSLKAP 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1064290784 385 KVLCHIDANPDNFLIFEKNNQteVRLIDWEYAGMQDPDLDIA 426
Cdd:PLN02421  182 VVFAHNDLLSGNLMLNEDEGK--LYFIDFEYGSYSYRGYDIG 221
 
Name Accession Description Interval E-value
LicC COG4750
CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid ...
 4-209 5.21e-55

CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


Pssm-ID: 443784 [Multi-domain]  Cd Length: 228  Bit Score: 184.26  E-value: 5.21e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784   4 KNAIILAAGLGRRTIPLNFETHKAFLEVNGEILIERLIVQLKEAGVSEIIIVIGYKKEQFRYLIDKYEVELIENDDFANS 83
Cdd:COG4750     1 MNAIILAAGLGSRFAPITYETPKGLLKVNGEPLIERQIRQLHEAGITDITVVVGYLKEQFEYLEDKYGVKLIYNPDYAEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784  84 NTLYSLSLAESYLSNSYIIPCDIWCATNPFtSKKDDSSWYMI-----------------GDISKSVTKLDNLSERLAVAF 146
Cdd:COG4750    81 NNISSLYLVRDKLGNTYICSSDNYLTENPF-EKYEYKSYYSAvykegetdewcvktnrdGRITKIEIGGKDGWIMLGHSY 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1064290784 147 IEQSDSIWIKQRLRELANNPSQQMLAWEELLVTD-GELAIPTFKNCEHFIQDINTFEDLIYLDD 209
Cdd:COG4750   160 WDKEDSKKFKEILEEEYEDPETRDLYWEDIYMDHiDELDMYARKYPAGDIYEFDSLDELREFDP 223
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
 234-434 2.01e-50

Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic choline kinases, as well as eukaryotic ethanolamine kinase. ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC), and sphingomyelin (SM). Although choline is the preferred substrate, ChoK also shows substantial activity towards ethanolamine and its N-methylated derivatives. Bacterial ChoK is also referred to as licA protein. ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate and displays negligible activity towards N-methylated derivatives of Etn. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. The ChoK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270700 [Multi-domain]  Cd Length: 152  Bit Score: 169.27  E-value: 2.01e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784 234 KNVFALKKGMTNRSFMFECKDKSYIMRIPGEGTDKLINREQEAEVYRVIAGESISDELIYISPEKGYKITSFIDGARNCD 313
Cdd:cd05151     1 ITIEPLKGGLTNKNYLVEVAGKKYVLRIPGAGTELLIDRENEKANSKAAAELGIAPEVIYFDPETGVKITEFIEGATLLT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784 314 SN--NKSDVSLCMKKLRSFHerglttshefdlfgeiefyeslrgnresiyedyqsvknrvltlksyiQLNIEKKVLCHID 391
Cdd:cd05151    81 NDfsDPENLERIAALLRKLH-----------------------------------------------SSPLEDLVLCHND 113

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1064290784 392 ANPDNFLIfeknNQTEVRLIDWEYAGMQDPDLDIAMFAIYSQY 434
Cdd:cd05151   114 LVPGNFLL----DDDRLYLIDWEYAGMNDPLFDLAALFSENNL 152
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 6-204 7.26e-35

Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.


Pssm-ID: 133014 [Multi-domain]  Cd Length: 229  Bit Score: 130.43  E-value: 7.26e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784   6 AIILAAGLGRRTIPLNFETHKAFLEVNGEILIERLIVQLKEAGVSEIIIVIGYKKEQFRYLIDKY-EVELIENDDFANSN 84
Cdd:cd02523     1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYpNIKFVYNPDYAETN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784  85 TLYSLSLAESYLS-NSYIIPCDIWCATNPF------------------------TSKKDDSSWYMIGDISKSVTKLDNLS 139
Cdd:cd02523    81 NIYSLYLARDFLDeDFLLLEGDVVFDPSILerllsspadnailvdkktkewedeYVKDLDDAGVLLGIISKAKNLEEIQG 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1064290784 140 ERLAVAFIEQSDSIWIKQRLRELANNPSQQMLaWEEL---LVTDGELAIptfKNCE-HFIQDINTFEDL 204
Cdd:cd02523   161 EYVGISKFSPEDADRLAEALEELIEAGRVNLY-YEDAlqrLISEEGVKV---KDISdGFWYEIDDLEDL 225
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
340-492 3.91e-33

Thiamine kinase or a related kinase [Coenzyme transport and metabolism];


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 123.35  E-value: 3.91e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784 340 EFDLFGEIEFYESLRgnresiYEDYQSVKNRVLTLKSYIQLNIEKKVLCHIDANPDNFLIfekNNQTEVRLIDWEYAGMQ 419
Cdd:COG0510    10 RFDLFARLERYLALG------PRDLPELLRRLEELERALAARPLPLVLCHGDLHPGNFLV---TDDGRLYLIDWEYAGLG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1064290784 420 DPDLDIAMFAIYSQYNREQIDFLIGAYFEEGCEERIRMKIYAYVATAGLLWSNWCEYK--QQLGVEFGDYAQSQY 492
Cdd:COG0510    81 DPAFDLAALLVEYGLSPEQAEELLEAYGFGRPTEELLRRLRAYRALADLLWALWALVRaaQEANGDLLKYLLRRL 155
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
6-102 1.95e-26

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 107.25  E-value: 1.95e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784   6 AIILAAGLGRRTIPLNFETHKAFLEVNGEILIERLIVQLKEAGVSEIIIVIGYKKEQFRYLIDKY--EVELIENDDFANS 83
Cdd:COG1213     2 AVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALARPgpDVTFVYNPDYDET 81

                          90
                  ....*....|....*....
gi 1064290784  84 NTLYSLSLAESYLSNSYII 102
Cdd:COG1213    82 NNIYSLWLAREALDEDFLL 100
Choline_kinase pfam01633
Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of ...
 253-428 9.45e-17

Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of phosphatidylcholine by the CDP-choline pathway. This alignment covers the protein kinase portion of the protein. The divergence of this family makes it very difficult to create a model that specifically predicts choline/ethanolamine kinases only. However if [add Pfam ID here for Choline_kinase_C] is also present then it is definitely a member of this family.


Pssm-ID: 396278 [Multi-domain]  Cd Length: 211  Bit Score: 78.85  E-value: 9.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784 253 KDKSYIMRIPGEGTDKLINREQEAEVYRVIAGESISDELIYISPEKGykITSFIDG-ARNCDSNNKSDVSLCM-KKLRSF 330
Cdd:pfam01633   1 SPRKVLLRIYGPGTELLINREDEIVNFALLSERGLGPKLYGFFPNGR--IEEFIPSrTLSTEDLRDPEISKLIaKRLAEL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784 331 HERGLTTSHEFDLFGEIEFYESL---RGNRESI-------YEDYQSVKNRVLTLKSYIQLNIEKKVLCHIDANPDNFLif 400
Cdd:pfam01633  79 HSLEMPGKKSPSLWKTMRKWLSLlknLGAPESVnkseqlkSINLEDLEKEINKLEKWLELLDSPIVFCHNDLQSGNIL-- 156

                         170       180
                  ....*....|....*....|....*...
gi 1064290784 401 EKNNQTEVRLIDWEYAGMQDPDLDIAMF 428
Cdd:pfam01633 157 LLNETKRLVLIDFEYASYNYRGFDIANH 184
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 6-108 2.05e-15

NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440821 [Multi-domain]  Cd Length: 238  Bit Score: 75.57  E-value: 2.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784   6 AIILAAGLGRRTIPLNFETHKAFLEVNGEILIERLIVQLKEAGVSEIIIVIGYKKEQFR-YLIDKY----EVELIENDDf 80
Cdd:COG1208     2 AVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEeYFGDGSrfgvRITYVDEGE- 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1064290784  81 aNSNTLYSLSLAESYLSNS--YIIPCDIWC 108
Cdd:COG1208    81 -PLGTGGALKRALPLLGDEpfLVLNGDILT 109
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
6-81 4.55e-15

CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 73.66  E-value: 4.55e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1064290784   6 AIILAAGLGRRtiplnFETHKAFLEVNGEILIERLIVQLKEAGVSEIIIVIGYKKEQFRYLIDKYEVELIENDDFA 81
Cdd:COG2068     6 AIILAAGASSR-----MGRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAGLGVRVVVNPDWE 76
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 6-64 4.44e-14

NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides.


Pssm-ID: 133024 [Multi-domain]  Cd Length: 217  Bit Score: 71.46  E-value: 4.44e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1064290784   6 AIILAAGLGRRTIPLNFETHKAFLEVNGEILIERLIVQLKEAGVSEIIIVIGYKKEQFR 64
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIE 59
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 6-105 9.83e-14

GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 69.51  E-value: 9.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784   6 AIILAAGLGRRtiplnFETHKAFLEVNGEILIERLIVQLKEAGVSEIIIVIGYKKEQFRYLIDKYEVELIENDDFAN--S 83
Cdd:cd04182     3 AIILAAGRSSR-----MGGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVVVINPDWEEgmS 77

                          90       100
                  ....*....|....*....|....*.
gi 1064290784  84 ntlYSLSLAESYLSNSY----IIPCD 105
Cdd:cd04182    78 ---SSLAAGLEALPADAdavlILLAD 100
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 6-106 1.17e-11

MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 62.98  E-value: 1.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784   6 AIILAAGLGRRtiplnFETHKAFLEVNGEILIERLIVQLKEAGvSEIIIVIGYkkEQFRYLIDKYEVELIENDDFAnSNT 85
Cdd:pfam12804   1 AVILAGGRSSR-----MGGDKALLPLGGKPLLERVLERLRPAG-DEVVVVAND--EEVLAALAGLGVPVVPDPDPG-QGP 71

                          90       100
                  ....*....|....*....|....
gi 1064290784  86 LYSLSLAESYLSNS---YIIPCDI 106
Cdd:pfam12804  72 LAGLLAALRAAPGAdavLVLACDM 95
ETNK_euk cd05157
Euykaryotic Ethanolamine kinase; ETNK catalyzes the transfer of the gamma-phosphoryl group ...
 242-473 2.41e-10

Euykaryotic Ethanolamine kinase; ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate, and displays negligible activity towards N-methylated derivatives of Etn. The Drosophila ETNK is implicated in development and neuronal function. Mammals contain two ETNK proteins, ETNK1 and ETNK2. ETNK1 selectively increases Etn uptake and phosphorylation, as well as PtdEtn synthesis. ETNK2 is found primarily in the liver and reproductive tissues. It plays a critical role in regulating placental hemostasis to support late embryonic development. It may also have a role in testicular maturation. ETNK is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270706 [Multi-domain]  Cd Length: 307  Bit Score: 61.83  E-value: 2.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784 242 GMTNRsfMFEC------KDKSYIMRIPGEGTDKLINREQEAEVYRVIAGESISDELiYISPEKGYkITSFIDGaRNCDSN 315
Cdd:cd05157     9 GITNA--LYKVtypsgdTPKTVLVRIYGPGTELLIDRDRELRILQLLSRAGIGPKL-YGRFENGR-VEEFLPG-RTLTPE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784 316 N--KSDVSLCM-KKLRSFHE----RGLTTSHEFDLFGEIE-FYESLRGNRESIYEDY--------QSVKNRVLTLKSYI- 378
Cdd:cd05157    84 DlrDPKISRLIaRRLAELHSivplGEIEGKKKPILWTTIRkWLDLAPEVFEDEKNKEkklekvdlERLRKELEWLEKWLe 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784 379 QLNIEKKVLCHIDANPDNFLIFEKNNQteVRLIDWEYAGMQDPDLDIA----------MFAIYSQY-NREQIDFLIGAYF 447
Cdd:cd05157   164 SLEKSPIVFCHNDLLYGNILYNEDDDS--VTFIDFEYAGPNPRAFDIAnhfcewagfyCVLDYSRYpTKEEQRNFLRAYL 241

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1064290784 448 EEGCE------------ERIRMKIYAYVATAGLLWSNW 473
Cdd:cd05157   242 ESLDGlpggeevseeevEKLYNEVNLFRLASHLFWGLW 279
ycfN_thiK TIGR02721
thiamine kinase; Members of this family are the ycfN gene product of Escherichia coli, now ...
 236-446 2.42e-10

thiamine kinase; Members of this family are the ycfN gene product of Escherichia coli, now identified as the salvage enzyme thiamine kinase (thiK), and additional proteobacterial homologs taken to be orthologs with equivalent function. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 274268 [Multi-domain]  Cd Length: 256  Bit Score: 60.88  E-value: 2.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784 236 VFALKKGMTNRSFMFECKDKSYIMRIPGEGTDKL-INREQEAEVYRVIAGESISDELIYISPekGYKITSFIDGARNCDS 314
Cdd:TIGR02721   1 VQTLSGGLTNRSWRIEHPGISFVWRPQSPVCKALgVDRQREYQILQALSALGLAPKPILVNE--HWLLVEWLEGEVITLD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784 315 NNKSDVSLC--MKKLRSFHERGLTtSHEFDLFGEIEFY-ESLRGNR-----ESIYEDYQSVKnrvltLKSYIQLniekkV 386
Cdd:TIGR02721  79 QFVALDLLLelAALLHQLHSQPRF-GYPLSLKARIAHYwLQIDPARrtpewLRLYKQFRSAP-----EPAPLPL-----A 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784 387 LCHIDANPDNFLIFEKNnqteVRLIDWEYAGMQDPDLDIAmfAIYSQYNREQIDFLIGAY 446
Cdd:TIGR02721 148 PLHMDVHAYNLVVTPQG----LKLIDWEYASDGDIALELA--AIIRANDEEQQQDFVQRY 201
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 6-64 7.76e-10

G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family is the long form of Glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.The long from enzymes also have a left-handed parallel helix domain at the c-terminus, whereas, th eshort form enzymes do not have this domain. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose.


Pssm-ID: 133032 [Multi-domain]  Cd Length: 236  Bit Score: 59.12  E-value: 7.76e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1064290784   6 AIILAAGLGRRTIPLNFETHKAFLEVNGEILIERLIVQLKEAGVSEIIIVIGYKKEQFR 64
Cdd:cd04189     3 GLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIK 61
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 5-64 3.69e-09

NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.


Pssm-ID: 133044 [Multi-domain]  Cd Length: 221  Bit Score: 56.81  E-value: 3.69e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784   5 NAIILAAGLGRRTIPLNFETHKAFLEVNGEILIERLIVQLKEAGVSEIIIVIGYKKEQFR 64
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIE 60
ChoK-like_euk cd14021
Euykaryotic Choline Kinase and similar proteins; This group is composed of eukaryotic choline ...
 242-428 3.64e-08

Euykaryotic Choline Kinase and similar proteins; This group is composed of eukaryotic choline kinase, ethanolamine kinase, and similar proteins. ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC), and sphingomyelin (SM). Although choline is the preferred substrate, ChoK also shows substantial activity towards ethanolamine and its N-methylated derivatives. ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate and displays negligible activity towards N-methylated derivatives of Etn. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. The ChoK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270923 [Multi-domain]  Cd Length: 229  Bit Score: 54.20  E-value: 3.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784 242 GMTNRSFMFECKD-------KSYIMRIPGEGTDKLINREQEAEVYRVIAGESISDELIYISPekGYKITSFIDGAR--NC 312
Cdd:cd14021     9 GLTNQVYKVSLKDesdslepKKVLFRIYGKYLSTLYDREKESEVFKILSEQGLGPKLIYKFD--GGRIEEYIDGRPltTD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784 313 DSNNKSDVSLCMKKLRSFHerglttshefdlfgeiefyeslrgnresiyedyqsvknrvltlksyiQLNIEKKVLCHIDA 392
Cdd:cd14021    87 ELRNPSVLTSIAKLLAKFH-----------------------------------------------KIKTPPVVFCHNDL 119

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1064290784 393 NPDNFLIFekNNQTEVRLIDWEYAGMQDPDLDIAMF 428
Cdd:cd14021   120 QENNILLT--NDQDGLRLIDFEYSGFNYRGYDIANF 153
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 6-75 5.85e-08

WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is involved in the biosynthesis, export or translocation of capsule. It is a subfamily of nucleotidyl transferases that transfer nucleotides onto phosphosugars.


Pssm-ID: 133065 [Multi-domain]  Cd Length: 223  Bit Score: 53.33  E-value: 5.85e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1064290784   6 AIILAAGLGRRTIPLNFETHKAFLEVNGEILIERLIVQLKEAGVSEIIIVIGYKKEQFR-YLIDKYEVELI 75
Cdd:cd06915     1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEeYFGDGYRGGIR 71
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 238-450 9.85e-08

Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance proteins, which confer resistance to various aminoglycosides they include: aminoglycoside 3'-phosphotransferase or kanamycin kinase / neomycin-kanamycin phosphotransferase and streptomycin 3''-kinase or streptomycin 3''-phosphotransferase. The aminoglycoside phosphotransferases inactivate aminoglycoside antibiotics via phosphorylation. This family also includes homoserine kinase. This family is related to fructosamine kinase pfam03881.


Pssm-ID: 426359 [Multi-domain]  Cd Length: 239  Bit Score: 52.89  E-value: 9.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784 238 ALKKGMTNRSFMFECKDKSYIMRIPgEGTDKLINREQEAEVYRVIAGESIS--------DELIYISpEKGYKITSFIDGA 309
Cdd:pfam01636   4 PISSGASNRTYLVTTGDGRYVLRLP-PPGRAAEELRRELALLRHLAAAGVPpvprvlagCTDAELL-GLPFLLMEYLPGE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784 310 rncDSNNKSDVSLCMKKLRSFHeRGLTTSHEFD-----LFGEIEFYESLRGNRESIYEDYQSVKNRVLTLKSYIQL---- 380
Cdd:pfam01636  82 ---VLARPLLPEERGALLEALG-RALARLHAVDpaalpLAGRLARLLELLRQLEAALARLLAAELLDRLEELEERLlaal 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1064290784 381 -----NIEKKVLCHIDANPDNFLIFEKNNQTEVrlIDWEYAGMQDPDLDIAMFA--IYSQYNREQIDFLIGAYFEEG 450
Cdd:pfam01636 158 lallpAELPPVLVHGDLHPGNLLVDPGGRVSGV--IDFEDAGLGDPAYDLAILLnsWGRELGAELLAAYLAAYGAFG 232
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 6-106 1.12e-07

NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.


Pssm-ID: 133048 [Multi-domain]  Cd Length: 220  Bit Score: 52.51  E-value: 1.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784   6 AIILAAGLGRRTIPLNFETHKAFLEVNGEILIERLIVQLKEAGVSEIIIVIGYKKEQFR-YLID----KYEVELIENDDF 80
Cdd:cd06426     1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEdYFGDgskfGVNISYVREDKP 80

                          90       100
                  ....*....|....*....|....*..
gi 1064290784  81 AnsNTLYSLSLAESYLSNSYIIP-CDI 106
Cdd:cd06426    81 L--GTAGALSLLPEKPTDPFLVMnGDI 105
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 6-79 1.91e-07

N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU). GlmU is an essential bacterial enzyme with both an acetyltransferase and an uridyltransferase activity which have been mapped to the C-terminal and N-terminal domains, respectively. This family represents the N-terminal uridyltransferase. GlmU performs the last two steps in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc), which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathways in Gram-positive and Gram-negative bacteria, respectively.


Pssm-ID: 133020 [Multi-domain]  Cd Length: 229  Bit Score: 52.13  E-value: 1.91e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1064290784   6 AIILAAGLGRRtipLNFETHKAFLEVNGEILIERLIVQLKEAGVSEIIIVIGYKKEQFRYLIDKYEVELIENDD 79
Cdd:cd02540     1 AVILAAGKGTR---MKSDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALANPNVEFVLQEE 71
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 5-71 2.56e-07

MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme molybdopterin-guanine dinucleotide biosynthesis protein A (MobA). All mononuclear molybdoenzymes bind molybdenum in complex with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by attachment of a GMP group to the terminal phosphate of molybdopterin to form molybdopterin guanine dinucleotide (MGD). This GMP attachment step is catalyzed by MobA, by linking a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide. This reaction requires GTP, MgCl2, and the MPT form of the cofactor. It is a reaction unique to prokaryotes, and therefore may represent a potential drug target.


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 50.65  E-value: 2.56e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1064290784   5 NAIILAAGLGRRtiplnFETHKAFLEVNGEILIERLIVQLKEAgVSEIIIVIG-----YKKEQFRYLIDKYE 71
Cdd:cd02503     2 TGVILAGGKSRR-----MGGDKALLELGGKPLLEHVLERLKPL-VDEVVISANrdqerYALLGVPVIPDEPP 67
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 6-71 3.77e-06

Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein A is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440509 [Multi-domain]  Cd Length: 188  Bit Score: 47.49  E-value: 3.77e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784   6 AIILAAGLGRRtiplnFETHKAFLEVNGEILIERLIVQLKEAgVSEIIIVI----GYKKEQFRYLIDKYE 71
Cdd:COG0746     7 GVILAGGRSRR-----MGQDKALLPLGGRPLLERVLERLRPQ-VDEVVIVAnrpeRYAALGVPVVPDDPP 70
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 5-76 3.99e-06

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 49.25  E-value: 3.99e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1064290784   5 NAIILAAGLGRRtipLNFETHKAFLEVNGEILIERLIVQLKEAGVSEIIIVIGYKKEQFRYLIDKYEVELIE 76
Cdd:COG1207     4 AVVILAAGKGTR---MKSKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALADLDVEFVL 72
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
 239-448 5.01e-06

Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction only];


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 48.19  E-value: 5.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784 239 LKKGMTNRSFMFECkDKSYIMRIPGEGTDKLINREQEAEVYRVIAGES----------ISDELIYISPekgYKITSFIDG 308
Cdd:COG3173    28 LSGGWSNLTYRLDT-GDRLVLRRPPRGLASAHDVRREARVLRALAPRLgvpvprplalGEDGEVIGAP---FYVMEWVEG 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784 309 ---ARNCDSNNKSDVSLCMKK----LRSFH-----ERGLTTSHEFDLFGEIEFYESLRGNRESIYEDYQSVKNRVLTlks 376
Cdd:COG3173   104 etlEDALPDLSPAERRALARAlgefLAALHavdpaAAGLADGRPEGLERQLARWRAQLRRALARTDDLPALRERLAA--- 180

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1064290784 377 YIQLNI---EKKVLCHIDANPDNfLIFEKNNQTEVRLIDWEYAGMQDPDLDIAMFAIYSQYN---REQIDFLIGAYFE 448
Cdd:COG3173   181 WLAANLpewGPPVLVHGDLRPGN-LLVDPDDGRLTAVIDWELATLGDPAADLAYLLLYWRLPddlLGPRAAFLAAYEE 257
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 5-74 6.37e-06

N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain and a C-terminal Lefthanded-beta-Helix fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes, such as cell lysis, defective cell wall, and failure of polarized growth and cell separation.


Pssm-ID: 133047 [Multi-domain]  Cd Length: 233  Bit Score: 47.59  E-value: 6.37e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784   5 NAIILAAGLGRRTIPLNFETHKAFLEVNGEILIERLIVQLKEAGVSEIIIVIGYKKEQFRYLIDKYEVEL 74
Cdd:cd06425     2 KALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEKKL 71
thiK PRK10271
thiamine kinase; Provisional
 389-481 2.50e-05

thiamine kinase; Provisional


Pssm-ID: 182349  Cd Length: 188  Bit Score: 45.12  E-value: 2.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784 389 HIDANPDNFLIfeknNQTEVRLIDWEYAGMQDPDLDIAMFAIYSQYNREQidfLIGAYFEEG--CEERIRMKIYAYVATA 466
Cdd:PRK10271   81 HMDVHAGNLVH----SASGLRLIDWEYAGDGDIALELAAVWVENTEQHRQ---LVNDYATRAkiDAAQLWRQVRRWFPWV 153

                          90
                  ....*....|....*.
gi 1064290784 467 GLLWSNWCEYK-QQLG 481
Cdd:PRK10271  154 LMLKAGWFEYRwRQTG 169
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 4-68 2.89e-05

Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose Pyrophosphorylase (UGPase) catalyzes a reversible production of UDP-Glucose and pyrophosphate (PPi) from glucose-1-phosphate and UTP. UDP-glucose plays pivotal roles in galactose utilization, in glycogen synthesis, and in the synthesis of the carbohydrate moieties of glycolipids , glycoproteins , and proteoglycans. UGPase is found in both prokaryotes and eukaryotes, although prokaryotic and eukaryotic forms of UGPase catalyze the same reaction, they share low sequence similarity.


Pssm-ID: 133021 [Multi-domain]  Cd Length: 267  Bit Score: 45.60  E-value: 2.89e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1064290784   4 KNAIILAAGLGRRTIPLNFETHKAFLEVNGEILIERLIVQLKEAGVSEIIIVIGYKKeqfRYLID 68
Cdd:cd02541     1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGK---RAIED 62
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-62 4.46e-05

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 45.98  E-value: 4.46e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1064290784   4 KNAIILAAGLGRRtipLNFETHKAFLEVNGEILIERLIVQLKEAGVSEIIIVIGYKKEQ 62
Cdd:PRK14354    3 RYAIILAAGKGTR---MKSKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEE 58
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 6-56 6.33e-05

CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 44.44  E-value: 6.33e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1064290784   6 AIILAAGLGRRtipLNFETHKAFLEVNGEILIERLIVQLKEAG-VSEIIIVI 56
Cdd:cd02516     3 AIILAAGSGSR---MGADIPKQFLELGGKPVLEHTLEAFLAHPaIDEIVVVV 51
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
6-68 7.44e-05

dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 44.70  E-value: 7.44e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1064290784   6 AIILAAGLGRRTIPLnfeTH---KAFLEVNGEILIERLIVQLKEAGVSEIIIVIG-YKKEQF-RYLID 68
Cdd:COG1209     3 GIILAGGSGTRLRPL---TLtvsKQLLPVYDKPMIYYPLSTLMLAGIREILIISTpEDGPQFeRLLGD 67
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 7-56 3.12e-04

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440824  Cd Length: 224  Bit Score: 42.04  E-value: 3.12e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1064290784   7 IILAAGLGRRtipLNFETHKAFLEVNGEILIERLIVQLKEAG-VSEIIIVI 56
Cdd:COG1211     1 IIPAAGSGSR---MGAGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVV 48
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
6-70 4.55e-04

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 41.66  E-value: 4.55e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1064290784   6 AIILAAGLGRRtipLNFETHKAFLEVNGEILIERLIVQLKEAG-VSEIIIVIGykKEQFRYLIDKY 70
Cdd:PRK00155    6 AIIPAAGKGSR---MGADRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVP--PDDRPDFAELL 66
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 9-76 1.21e-03

GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP:adenosylcobinamide-phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441867 [Multi-domain]  Cd Length: 185  Bit Score: 39.87  E-value: 1.21e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1064290784   9 LAAGLGRRtipLNFeTHKAFLEVNGEILIERLIVQLKEAGVSEIIIVIGYKKEQFRYLIDKYEVELIE 76
Cdd:COG2266     1 MAGGKGTR---LGG-GEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSPNTPKTREYLKERGVEVIE 64
PRK14489 PRK14489
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; ...
 6-68 2.60e-03

putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; Provisional


Pssm-ID: 237727 [Multi-domain]  Cd Length: 366  Bit Score: 40.12  E-value: 2.60e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1064290784   6 AIILAAGLGRRTIPLNfethKAFLEVNGEILIERLIVQLKEAgVSEIIIVIGYKKEQFRYLID 68
Cdd:PRK14489    8 GVILAGGLSRRMNGRD----KALILLGGKPLIERVVDRLRPQ-FARIHLNINRDPARYQDLFP 65
APH cd05150
Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group ...
 282-432 4.96e-03

Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group from ATP to aminoglycoside antibiotics such as kanamycin, streptomycin, neomycin, and gentamicin, among others. The aminoglycoside antibiotics target the 30S ribosome and promote miscoding, leading to the production of defective proteins which insert into the bacterial membrane, resulting in membrane damage and the ultimate demise of the bacterium. Phosphorylation of the aminoglycoside antibiotics results in their inactivation, leading to bacterial antibiotic resistance. The APH gene is found on transposons and plasmids and is thought to have originated as a self-defense mechanism used by microorganisms that produce the antibiotics. The APH subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270699 [Multi-domain]  Cd Length: 244  Bit Score: 38.72  E-value: 4.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784 282 IAGESISDELIYISPEKgyKITSFIDGAR--------NCDSNNKSDVSLcmKKLRSFHERGLTTSHEFDlfgeiefyESL 353
Cdd:cd05150    74 LPGRDAASLEPLLDPER--LVDLLAEALRalhslpiaDCPFDRRLDARL--AEARARVEAGLVDEDDFD--------EER 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784 354 RG-NRESIYEDYQsvKNRVLTlksyiqlniEKKVLCHIDANPDNFLIfekNNQTEVRLIDWEYAGMQDPDLDIAmFAIYS 432
Cdd:cd05150   142 QGrTAEELLAELE--ATRPAE---------EDLVVTHGDACLPNIIL---DPGRFSGFIDLGRLGVADRYQDLA-LAVRS 206
PLN02421 PLN02421
phosphotransferase, alcohol group as acceptor/kinase
 242-426 5.16e-03

phosphotransferase, alcohol group as acceptor/kinase


Pssm-ID: 215231 [Multi-domain]  Cd Length: 330  Bit Score: 38.95  E-value: 5.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784 242 GMTNRSFMFECKDK-----SYIMRIPGEGTDKLINREQEAEVYRVIAGESISDELIYISpeKGYKITSFIDgARNCDSNN 316
Cdd:PLN02421   25 GITNLLLKVSVKEEngnevSVTVRLFGPNTDYVIDRERELQAIKYLSAAGFGAKLLGVF--GNGMIQSFIN-ARTLTPSD 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784 317 KSD---VSLCMKKLRSFHERGLTTSHEFDLFGEI-EFYESLRG------NRESIYED--YQSVKNRVLTLKSYIQLNIEK 384
Cdd:PLN02421  102 MRKpkvAAEIAKELRRLHQVEIPGSKEPQLWNDIfKFYEKASTvkfedpEKQKKYETisFEELRDEIVELKEITDSLKAP 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1064290784 385 KVLCHIDANPDNFLIFEKNNQteVRLIDWEYAGMQDPDLDIA 426
Cdd:PLN02421  182 VVFAHNDLLSGNLMLNEDEGK--LYFIDFEYGSYSYRGYDIG 221
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 6-62 5.76e-03

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 39.07  E-value: 5.76e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1064290784   6 AIILAAGLGRRtipLNFETHKAFLEVNGEILIERLIVQLKEAGVSEIIIVIGYKKEQ 62
Cdd:PRK14353    8 AIILAAGEGTR---MKSSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEA 61
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
 386-426 7.93e-03

Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ChoK, ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). The members of this family catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides and macrolides, leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. The APH/ChoK family is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270690 [Multi-domain]  Cd Length: 158  Bit Score: 37.28  E-value: 7.93e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1064290784 386 VLCHIDANPDNFLIFEKNNQTEvrLIDWEYAGMQDPDLDIA 426
Cdd:cd05120   112 VLTHGDLHPGNILVKPDGKLSG--IIDWEFAGYGPPAFDYA 150
ACAD10_11_N-like cd05154
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ...
 386-431 8.25e-03

N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This subfamily is composed of the N-terminal domains of vertebrate ACAD10 and ACAD11, and similar uncharacterized bacterial and eukaryotic proteins. ACADs are a family of flavoproteins that are involved in the beta-oxidation of fatty acyl-CoA derivatives. ACAD deficiency can cause metabolic disorders including muscle fatigue, hypoglycemia, and hepatic lipidosis. There are at least 11 distinct ACADs, some of which show distinct substrate specificities to either straight-chain or branched-chain fatty acids. ACAD10 is widely expressed in human tissues and highly expressed in liver, kidney, pancreas, and spleen. ACAD10 and ACAD11 are both significantly expressed in human brain tissues. They contain a long N-terminal domain with similarity to phosphotransferases with a Protein Kinase fold, which is absent in other ACADs. They may exhibit multiple functions in acyl-CoA oxidation pathways. ACAD11 utilizes substrates with carbon chain lengths of 20 to 26, with optimal activity towards C22CoA. ACAD10 may be associated with an increased risk in type II diabetes. The ACAD10/11-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270703 [Multi-domain]  Cd Length: 254  Bit Score: 37.98  E-value: 8.25e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1064290784 386 VLCHIDANPDNFLIfekNNQTEVR-LIDWEYAGMQDPDLDIAMFAIY 431
Cdd:cd05154   178 VLVHGDFRLGNLLF---DPDGRVTaVLDWELATLGDPLEDLAWLLAR 221
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 6-108 8.44e-03

Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 38.00  E-value: 8.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064290784   6 AIILAAGLGRRTIPLNFETHK-AFLEVNGEILIERLIVQLKEAGVSEIIIVIGYKKEQ--FRYLIDKYEVELIENDDFAN 82
Cdd:pfam00483   2 AIILAGGSGTRLWPLTRTLAKpLVPVGGKYPLIDYPLSRLANAGIREIIVILTQEHRFmlNELLGDGSKFGVQITYALQP 81

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1064290784  83 S--NTLYSLSLAESYLSNSY----IIPCDIWC 108
Cdd:pfam00483  82 EgkGTAPAVALAADFLGDEKsdvlVLGGDHIY 113
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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